Lipolytic esterases in staphylococci.
Staphylococci split a wide range of lipid substrates by production of an enzyme complex with two main components (i) a lipase acting optimally on fat-soluble glycerides, and (ii) an esterase acting optimally on water-soluble esters. The action is dependent upon carbon chain length, interfacial dispersion, solubility, and pH of substrate and end products. The esterase is less susceptible to organophosphorus inhibitors than mammalian esterases. There is no apparent correlation between lipolysis and markers of pathogenicity such as production of coagulase and toxin, but the possession of a flexible lipolytic mechanism might account for the persistence of staphylococci in the fatty secretions of mammalian skin.
D004950:Esterases / Q000032:analysis / Q000037:antagonists & inhibitors / Q000378:metabolism*; D005989:Glycerides / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008365:Manometry; D013210:Staphylococcus / Q000201:enzymology*
D005989:Glycerides; D004950:Esterases; D008049:Lipase